ID TOP1_ECOLI STANDARD; PRT; 865 AA. AC P06612; DT 01-JAN-1988 (Rel. 06, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) DE (Untwisting enzyme) (Swivelase). GN Name=topA; Synonyms=supX; OrderedLocusNames=b1274; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87141163; PubMed=3029379; RA Tse-Dinh Y.-C., Wang J.C.; RT "Complete nucleotide sequence of the topA gene encoding Escherichia RT coli DNA topoisomerase I."; RL J. Mol. Biol. 191:321-331(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RA Lynch D.A., Wang J.C.; RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=97251357; PubMed=9097039; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 698-865. RX MEDLINE=87194810; PubMed=3032952; RA Ostrowski J., Jagura-Burdzy G., Kredich N.M.; RT "DNA sequences of the cysB regions of Salmonella typhimurium and RT Escherichia coli."; RL J. Biol. Chem. 262:5999-6005(1987). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-590. RX MEDLINE=94159070; PubMed=8114910; DOI=10.1038/367138a0; RA Lima C.D., Wang J.C., Mondragon A.; RT "Three-dimensional structure of the 67K N-terminal fragment of E. coli RT DNA topoisomerase I."; RL Nature 367:138-146(1994). RN [7] RP STRUCTURE BY NMR OF 745-865. RX MEDLINE=95298771; PubMed=7779808; RA Yu L., Zhu C.-X., Tse-Dinh Y.-C., Fesik S.W.; RT "Solution structure of the C-terminal single-stranded DNA-binding RT domain of Escherichia coli topoisomerase I."; RL Biochemistry 34:7622-7628(1995). CC -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the CC conversion of one topological isomer of DNA to another. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. CC -!- SUBUNIT: Monomer. CC -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA CC backbone bond, it simultaneously forms a protein-DNA link, in CC which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus CC at one end of the enzyme-severed DNA strand. CC -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04475; CAA28164.1; -; Genomic_DNA. DR EMBL; M15041; AAA23641.1; -; Genomic_DNA. DR EMBL; U00096; AAC74356.1; -; Genomic_DNA. DR EMBL; D90764; BAA14811.1; -; Genomic_DNA. DR EMBL; D90765; BAA14826.1; -; Genomic_DNA. DR PIR; E64875; ISECTP. DR PDB; 1CY0; X-ray; A=1-597. DR PDB; 1CY1; X-ray; A=1-597. DR PDB; 1CY2; X-ray; A=1-597. DR PDB; 1CY4; X-ray; A=1-597. DR PDB; 1CY6; X-ray; A=1-597. DR PDB; 1CY7; X-ray; A=1-597. DR PDB; 1CY8; X-ray; A=1-597. DR PDB; 1CY9; X-ray; A/B=214-477. DR PDB; 1CYY; X-ray; A/B=214-477. DR PDB; 1ECL; X-ray; @=1-597. DR PDB; 1MW8; X-ray; X=1-592. DR PDB; 1MW9; X-ray; X=1-592. DR PDB; 1YUA; NMR; @=745-865. DR ECO2DBASE; I115.0; 6TH EDITION. DR EchoBASE; EB1006; -. DR EcoGene; EG11013; topA. DR LinkHub; P06612; -. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR003601; DNA_topI_ATP_bd. DR InterPro; IPR005733; DNA_topI_bact. DR InterPro; IPR003602; DNA_topI_DNA_bd. DR InterPro; IPR000380; DNA_tpisomrase. DR InterPro; IPR006171; Toprim_dom. DR InterPro; IPR006154; Toprim_sub. DR PANTHER; PTHR11390; DNA_tpisomrase; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. KW 3D-structure; Complete proteome; DNA-binding; Isomerase; KW Metal-binding; Repeat; Topoisomerase; Zinc; Zinc-finger. FT ZN_FING 599 630 C4-type 1. FT ZN_FING 662 689 C4-type 2. FT ZN_FING 711 736 C4-type 3. FT ACT_SITE 319 319 DNA cleavage. FT CONFLICT 787 787 P -> R (in Ref. 5). FT STRAND 4 8 FT HELIX 11 18 FT TURN 19 20 FT TURN 23 24 FT STRAND 25 29 FT STRAND 35 36 FT HELIX 65 71 FT STRAND 73 74 FT TURN 75 79 FT STRAND 80 81 FT STRAND 84 85 FT TURN 87 89 FT HELIX 90 102 FT STRAND 105 108 FT HELIX 114 127 FT HELIX 131 133 FT STRAND 134 136 FT HELIX 144 152 FT STRAND 155 155 FT HELIX 159 186 FT TURN 187 187 FT TURN 189 190 FT TURN 195 196 FT HELIX 197 212 FT TURN 213 213 FT STRAND 218 227 FT TURN 229 230 FT STRAND 233 241 FT TURN 242 243 FT STRAND 244 245 FT HELIX 251 263 FT STRAND 266 278 FT STRAND 284 284 FT HELIX 286 297 FT HELIX 301 313 FT TURN 314 315 FT STRAND 317 317 FT HELIX 329 342 FT TURN 343 343 FT HELIX 345 347 FT STRAND 368 368 FT STRAND 370 370 FT TURN 373 374 FT HELIX 377 379 FT HELIX 385 401 FT TURN 402 402 FT STRAND 406 417 FT TURN 418 419 FT STRAND 420 431 FT HELIX 433 436 FT TURN 437 437 FT TURN 455 456 FT STRAND 458 470 FT HELIX 479 488 FT TURN 489 490 FT TURN 494 496 FT HELIX 497 506 FT TURN 507 508 FT STRAND 510 513 FT TURN 514 515 FT STRAND 516 519 FT HELIX 521 533 FT HELIX 535 538 FT HELIX 540 554 FT TURN 555 556 FT HELIX 560 578 FT TURN 579 579 FT HELIX 582 584 FT TURN 585 585 FT STRAND 756 762 FT STRAND 769 773 FT STRAND 780 783 FT TURN 784 787 FT STRAND 796 796 FT HELIX 797 802 FT TURN 803 806 FT TURN 810 811 FT HELIX 812 816 FT TURN 822 823 FT STRAND 827 832 FT TURN 833 836 FT STRAND 837 842 FT TURN 845 846 FT STRAND 853 855 FT STRAND 860 860 SQ SEQUENCE 865 AA; 97350 MW; 8C13F767FE5B178C CRC64; MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG WSAFYVDGKW VEGKK //